8) The field of proteomics is built off the ability to quickly identify proteins

Question

8) The field of proteomics is built off the ability to quickly identify proteins in complicated mixtures and finger print them so that you know who is present and at what quantity. Recent work has hypothesized and found evidence for variation in ribosomes such that not all ribosomes are identical and this heterogeneity leads to specialization that can provide added layers of regulation and control. Data have provided evidence that certain ribosomes specialize in the translation of a subset of mRNAs. Consider this problem of ribosome heterogeneity Propose an experiment that might let you look at this type of variability within ribosomes that are otherwise highly similar. Question 7 above can provide insight into one possible solution but there are several potential approaches to probe this issue.

Explanation / Answer

RIBOSOME HETEROGENEITY: its a another level of complexity in bacterial translation regulation.

HIGHLIGHTS

Bacterial ribosomes have an intrinsic regulatory capacity.

Ribosomes can vary in their protein and/or rRNA complement.

Variations in rRNA and r-protein modifications likewise could lead to heterogeneity

. Heterogeneous ribosomes can exhibit a functional specificity.

Translation of the mRNA-encoded genetic information into proteins is catalyzed by the intricate ribonucleoprotein machine, the ribosome. Historically, the bacterial ribosome is viewed as an unchangeable entity, constantly equipped with the entire complement of RNAs and proteins. Conversely, several lines of evidence indicate the presence of functional selective ribosomal subpopulations that exhibit variations in the RNA or the protein components and modulate the translational program in response to environmental changes. Here, we summarize these findings, which raise the functional status of the ribosome from a protein synthesis machinery only to a regulatory hub that integrates environmental cues in the process of protein synthesis, thereby adding an additional level of complexity to the regulation of gene expression.

ribosomes specialised in the translation of subset of mRNAs ,it could be due to

Genome duplication in eukaryotes created paralog pairs of ribosomal proteins (RPs) that show high sequence similarity/identity. However, individual paralogs can confer vastly different effects upon cellular processes, e.g., specific yeast paralogs regulate actin organization, bud site selection, and mRNA localization, although how specificity is conferred is unknown. Changes in the RP composition of ribosomes might allow for specialized translation of different subsets of mRNAs, yet it is unclear whether specialized ribosomes exist and if paralog specificity controls translation. Using translatome analyses, we show that the translation of mitochondrial proteins is highly down-regulated in yeast lacking RP paralogs required for normal mitochondrial function (e.g., RPL1b). Although RPL1a and RPL1b encode identical proteins, Rpl1b-containing ribosomes confer more efficient translation of respiration-related proteins. Thus, ribosomes varying in RP composition may confer specialized functions, and RP paralog specificity defines a novel means of translational control.

Although ribosomes were once conceptualized as uniform, fixed molecular machines that perform translation, it is now known that structural variations generate ribosome heterogeneity. For example, ribosomal RNA and ribosomal proteins (RPs) differ in their modification and composition within ribosomes to affect translation

so from the above conclusion it can eaisly say that ribosomes differs that their heterogeniety due to the enivironmental changes where proteomics arent beacuse of it application r ability itself in identification of protien amd theirs stability.....

so proteomics can be understood by

he focus of proteomics is a biological group called the proteome. The proteome is dynamic, defined as the set of proteins expressed in a specific cell, given a particular set of conditions. Within a given human proteome, the number of proteins can be as large as 2 million.

Proteins themselves are macromolecules: long chains of amino acids. This amino acid chain is constructed when the cellular machinery of the ribosome translates RNA transcripts from DNA in the cell's nucleus.  The transfer of information within cells commonly follows this path, from DNA to RNA to protein.

Proteins can be organized in four structural levels:

Each level of protein structure is essential to the finished molecule's function. The primary sequence of the amino acid chain determines where secondary structures will form, as well as the overall shape of the final 3D conformation. The 3D conformation of each small peptide or subunit determines the final structure and function of a protein conglomerate.

There are many different subdivisions of proteomics, including:

Proteomics has both a physical laboratory component and a computational component. These two parts are often linked together; at times data derived from laboratory work can be fed directly into sequence and structure prediction algorithms. Mass spectrometry of multiple types is used most frequently for this purpose.

Proteomics involves the applications of technologies for the identication and quantication of overall proteins present content of a cell, tissue or an organism. It supplements the other “omics” technologies such as genomic and transcriptomics to expound the identity of proteins of an organism, and to cognize the structure and functions of a particular protein. Proteomics-based technologies are utilized in various capacities for different research settings such as detection of various diagnostic markers, candidates for vaccine production, understanding pathogenicity mechanisms, alteration of expression patterns in response to different signals and interpretation of functional protein pathways in different diseases. Proteomics is practically intricate because it includes the analysis and categorization of overall protein signatures of a genome.

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